ID RMLB_MYCTU Reviewed; 331 AA.
AC O06329; L0TFH5; Q7D5I4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 01-MAY-2013, entry version 95.
DE RecName: Full=dTDP-glucose 4,6-dehydratase;
DE EC=4.2.1.46;
GN Name=rmlB; Synonyms=rfbB; OrderedLocusNames=Rv3464, MT3570;
OS Mycobacterium tuberculosis.
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [3]
RP FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16472764; DOI=10.1016/j.bbrc.2006.01.130;
RA Li W., Xin Y., McNeil M.R., Ma Y.;
RT "rmlB and rmlC genes are essential for growth of mycobacteria.";
RL Biochem. Biophys. Res. Commun. 342:170-178(2006).
CC -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form
CC dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving
CC oxidation, dehydration and reduction. Involved in the biosynthesis
CC of the dTDP-L-rhamnose which is a component of the critical
CC linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which
CC connects the galactan region of arabinogalactan to peptidoglycan
CC via a phosphodiester linkage.
CC -!- CATALYTIC ACTIVITY: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-
CC alpha-D-glucose + H(2)O.
CC -!- COFACTOR: Binds 1 NAD ion per monomer (By similarity).
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the sugar epimerase family. dTDP-glucose
CC dehydratase subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BX842583; CAB08730.1; -; Genomic_DNA.
DR EMBL; AE000516; AAK47910.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46286.1; -; Genomic_DNA.
DR PIR; E70566; E70566.
DR RefSeq; NP_217981.1; NC_000962.3.
DR RefSeq; NP_338096.1; NC_002755.2.
DR RefSeq; YP_006516953.1; NC_018143.1.
DR HSSP; P95780; 1KEP.
DR ProteinModelPortal; O06329; -.
DR SMR; O06329; 3-326.
DR STRING; 83332.Rv3464; -.
DR PRIDE; O06329; -.
DR EnsemblBacteria; AAK47910; AAK47910; MT3570.
DR GeneID; 13317071; -.
DR GeneID; 887332; -.
DR GeneID; 926625; -.
DR KEGG; mtc:MT3570; -.
DR KEGG; mtu:Rv3464; -.
DR KEGG; mtv:RVBD_3464; -.
DR PATRIC; 18129579; VBIMycTub22151_3885.
DR TubercuList; Rv3464; -.
DR eggNOG; COG1088; -.
DR HOGENOM; HOG000168006; -.
DR KO; K01710; -.
DR OMA; AYNDARY; -.
DR ProtClustDB; CLSK792508; -.
DR UniPathway; UPA00124; -.
DR GO; GO:0005618; C:cell wall; IDA:MTBBASE.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IGI:UniProtKB.
DR GO; GO:0070404; F:NADH binding; ISS:UniProtKB.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IDA:MTBBASE.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IGI:UniProtKB.
DR GO; GO:0040007; P:growth; IDA:MTBBASE.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR10366:SF41; PTHR10366:SF41; 1.
DR Pfam; PF01370; Epimerase; 1.
DR TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Lyase; NAD; Reference proteome.
FT CHAIN 1 331 dTDP-glucose 4,6-dehydratase.
FT /FTId=PRO_0000395348.
FT NP_BIND 7 13 NAD (Potential).
FT NP_BIND 33 36 NAD (By similarity).
FT NP_BIND 57 58 NAD (By similarity).
FT NP_BIND 147 151 NAD (By similarity).
FT REGION 120 122 Substrate binding (By similarity).
FT REGION 186 187 Substrate binding (By similarity).
FT REGION 202 204 Substrate binding (By similarity).
FT REGION 270 273 Substrate binding (By similarity).
FT ACT_SITE 121 121 Proton donor (By similarity).
FT ACT_SITE 122 122 Proton acceptor (By similarity).
FT ACT_SITE 147 147 Proton acceptor (Probable).
FT BINDING 81 81 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 96 96 NAD (By similarity).
FT BINDING 176 176 Substrate (By similarity).
FT BINDING 177 177 NAD; via amide nitrogen (By similarity).
FT BINDING 211 211 Substrate (By similarity).
FT BINDING 246 246 Substrate (By similarity).
SQ SEQUENCE 331 AA; 37558 MW; 10652C75423082D2 CRC64;
MRLLVTGGAG FIGTNFVHSA VREHPDDAVT VLDALTYAGR RESLADVEDA IRLVQGDITD
AELVSQLVAE SDAVVHFAAE SHVDNALDNP EPFLHTNVIG TFTILEAVRR HGVRLHHIST
DEVYGDLELD DRARFTESTP YNPSSPYSAT KAGADMLVRA WVRSYGVRAT ISNCSNNYGP
YQHVEKFIPR QITNVLTGRR PKLYGAGANV RDWIHVDDHN SAVRRILDRG RIGRTYLISS
EGERDNLTVL RTLLRLMDRD PDDFDHVTDR VGHDLRYAID PSTLYDELCW APKHTDFEEG
LRTTIDWYRD NESWWRPLKD ATEARYQERG Q
//
